ID C9R9G7_AMMDK Unreviewed; 421 AA. AC C9R9G7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 24-JAN-2024, entry version 65. DE SubName: Full=Ribulose bisphosphate carboxylase, type III {ECO:0000313|EMBL:ACX52946.1}; DE EC=4.1.1.39 {ECO:0000313|EMBL:ACX52946.1}; GN OrderedLocusNames=Adeg_1863 {ECO:0000313|EMBL:ACX52946.1}; OS Ammonifex degensii (strain DSM 10501 / KC4). OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Ammonifex. OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52946.1, ECO:0000313|Proteomes:UP000002620}; RN [1] {ECO:0000313|EMBL:ACX52946.1, ECO:0000313|Proteomes:UP000002620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620}; RG US DOE Joint Genome Institute; RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A., RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.; RT "Complete sequence of chromosome of Ammonifex degensii KC4."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. CC {ECO:0000256|RuleBase:RU003834}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001785; ACX52946.1; -; Genomic_DNA. DR RefSeq; WP_015739823.1; NC_013385.1. DR AlphaFoldDB; C9R9G7; -. DR STRING; 429009.Adeg_1863; -. DR KEGG; adg:Adeg_1863; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_1_9; -. DR OrthoDB; 9770811at2; -. DR Proteomes; UP000002620; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015977; P:carbon fixation; IEA:InterPro. DR CDD; cd08213; RuBisCO_large_III; 1. DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1. DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1. DR HAMAP; MF_01133; RuBisCO_L_type3; 1. DR InterPro; IPR033966; RuBisCO. DR InterPro; IPR017712; RuBisCO_III. DR InterPro; IPR000685; RuBisCO_lsu_C. DR InterPro; IPR036376; RuBisCO_lsu_C_sf. DR InterPro; IPR017443; RuBisCO_lsu_fd_N. DR InterPro; IPR036422; RuBisCO_lsu_N_sf. DR NCBIfam; TIGR03326; rubisco_III; 1. DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1. DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SFLD; SFLDS00014; RuBisCO; 1. DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1. DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1. DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1. PE 3: Inferred from homology; KW Lyase {ECO:0000313|EMBL:ACX52946.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002620}. FT DOMAIN 5..118 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 129..419 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" SQ SEQUENCE 421 AA; 45345 MW; 0F22360AF434DC49 CRC64; MRYSDFVELN YTPSPSDCLA CFYVEPAEGV DIYEAAGAVA SESSIGTWTD VATMKPRIWE ELRARVYAIE GNVVKIAYPA ALFEPGNIPQ YLSSIAGNIF GMKAVKNLRL LDISFPPELV SGSLGPAFGV QGVRETLGIY GRPLVGTIVK PKLGLSPREQ AEVVYEALVG GLDLVKDDEN LTSQPFSPFE ERVKRSLEAC ARAEAEAGEK KVYLPNVTAE TEEMIRRAEL VKREGGRYVM VDIVTAGFSG LLSLRKANLG LIIHAHRAMY ASFARNRRHG ISMLVLAKLA RLAGVDQLHI GTVVGKMEGD KEDVLRCHAA LGNASPVSGD LLRPQDWGEI KPVLSVASGG LHPGHIPDLI SIFGVDCVLQ FGGGVHGHPR GTRAGASAVR AAVEAATSGQ SFQEVARREK TLEEAIMHWG G //